|
KMID : 0379120040320020119
|
|
Korean Journal of Mycology
2004 Volume.32 No. 2 p.119 ~ p.124
|
|
|
Characterization of a Fibrinolytic Metalloenzyme from a Wild Mushroom, Tricholoma sejunctum
|
|
Kim Jun-Ho
Jo Seung-Ku
|
|
|
Abstract
|
|
|
|
Metalloenzyme was purified from the fruiting bodies of Tricholoma sejunctum. MALDI-TOF and ICP/MS analyses revealed that the enzyme had a molecular weight of 18788.25 and includes $Zn^{2+}$ ion. The N-terminal amino acid sequence of the enzyme was Ala-Thr-Tyr-Lys-Ile-X-Ser-Ala-Thr-His-Gln-X-X-Leu-Val. The activity of the enzyme was inhibited by EDTA and 1,10-phenanthroline, indicating that the enzyme was a metalloprotease. No inhibition was found with E-64 and pepstatin. It has broad substrate specificity for synthetic peptides. The enzyme was stable up to $40^{\circ}C$. The activity of the enzyme was increased by $Zn^{2+}$ and $Co^{2+}$, while it was totally inhibited by $Hg^{2+}$. The enzyme hydrolyzes $A{\alpha}$ subunit of human fibrinogen but did not show any reactivity for $B{\beta}$ and ${\gamma}$ form of human fibrinogen.
|
|
|
KEYWORD
|
|
|
Fibrin plate assay, Fibrinolytic enzyme, Tricholoma sejunctum
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
 
|